Date of Award

1-1966

Document Type

Thesis - Restricted

Degree Name

Master of Science (MS)

Department

Medical

First Advisor

Robert J. Peanasky

Second Advisor

M. Laskowski

Third Advisor

Daniel T. Haworth

Abstract

Ascaris Lumbricoides in its natural habitat is subject to attack by proteolytic enzymes against which it has effective defenses.

Mendel and Blood (53) recognized the presence of trypsin and pepsin inhibitors in Ascaris as well as a chymotrypsin inhibitor since a crude pancreatic proteinase preparation was almost completely inhibited by tissue extracts.

In 1941 Collier (16) partially purified an extract of Ascaris and found that it inhibited trypsin and pepsin but not papain.

In 1957 Green (30) first proposed that the inhibitors of trypsin and chymotrypsin in Ascaris were independent. The chymotrypsin inhibitor was separated from the trypsin inhibitor by continuous flow paper electrophoresis at pH 5.05 in acetate buffer by Peanasky and Laskowski (56). The chymotrypsin inhibitor was crystallized and shown to inhibit chymotrypsin ∝ and B but not trypsin. At the time the present work was in progress, Pudles and Rola (58) reported in an abstract on the separation of these two inhibitors by ammonium sulfate fractionation and further purification of the two inhibitors on Sephadox G-75, carboxymethyl and diethylaminoethyl-cellulose. No details of this work have been published.

The purpose of this project was to obtain a purified preparation of the specific trypsin inhibitor from Ascaris and to compare its properties with the specific chymotrypsin inhibitor of the same source and with the trypsin inhibitors from pancreas, colostrum, and soybeans which inhibit both trypsin and chymotrypsin.

Comments

The original document was water damaged. This is the best copy available.

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